Abstract
Summary A non-dialyzable inhibitor of protein synthesis has been partially purified from Ehrlich ascites tumor cells. Preparations of this inhibitor have no effect on the initial rate of protein synthesis in rabbit reticulocyte lysates but cause a partial shut-off of amino acid incorporation after a lag period. The inhibitor has no appreciable endonuclease activity towards reticulocyte polysomes but under conditions of protein synthesis if causes disaggregation of polysomes. The effect of the inhibition can be overcome by the initiation factor which forms a ternary complex with Met-tRNA f and GTP and which binds of 40S ribosomal subunits. These results suggest that the Ehrlich ascites inhibitor is very similar to an inhibitor previously identified in reticulocytes.
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